Tethering of ferredoxin:NADP+ oxidoreductase to thylakoid membranes is mediated by novel chloroplast protein TROL.

Working in tandem, two photosystems in the chloroplast thylakoid membranes produce a linear electron flow from H(2)O to NADP(+). Final electron transfer from ferredoxin to NADP(+) is accomplished by a flavoenzyme ferredoxin:NADP(+) oxidoreductase (FNR). Here we describe TROL (thylakoid rhodanese-like protein), a nuclear-encoded component of thylakoid membranes that is required for tethering of FNR and sustaining efficient linear electron flow (LEF) in vascular plants. TROL consists of two distinct modules; a centrally positioned rhodanese-like domain and a C-terminal hydrophobic FNR binding region. Analysis of Arabidopsis mutant lines indicates that, in the absence of TROL, relative electron transport rates at high-light intensities are severely lowered accompanied with significant increase in non-photochemical quenching (NPQ). Thus, TROL might represent a missing thylakoid membrane docking site for a complex between FNR, ferredoxin and NADP(+). Such association might be necessary for maintaining photosynthetic redox poise and enhancement of the NPQ.

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